Information on EC 1.20.1.1 - phosphonate dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.20.1.1
-
RECOMMENDED NAME
GeneOntology No.
phosphonate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphonate + NAD+ + H2O = phosphate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphonate:NAD+ oxidoreductase
NADP+ is a poor substitute for NAD+ in the enzyme from Pseudomonas stutzeri WM88.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-35-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hydroxypyruvate + NAD+
pyruvate + NADH
show the reaction diagram
very poor substrate
-
?
phosphite + H2O + NAD+
phosphate + NADH + H+
show the reaction diagram
phosphite + H2O + NADP+
phosphate + NADPH + H+
show the reaction diagram
phosphonate + H2O + NAD+
phosphate + NADH
show the reaction diagram
phosphonate + H2O + NADP+
phosphate + NADPH
show the reaction diagram
phosphonate + NAD+ + H2O
phosphate + NADH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphite + H2O + NAD+
phosphate + NADH + H+
show the reaction diagram
phosphonate + H2O + NAD+
phosphate + NADH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EDTA
1 mM, about 155% of initial activity
Fe3+
1 mM, about 150% of initial activity
Mg2+
1 mM, about 125% of initial activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Bromoethylamine
-
1 mM NAD+ protects against inactivation
arsenite
Cd2+
1 mM, no residual activity
Cu2+
1 mM, about 55% of initial activity
D,L-hydroxyisocapronate
-
-
-
D-2-hydroxy-4-methylvalerate
-
-
D-glycerate
-
-
diethyl dicarbonate
-
-
Mn2+
1 mM, about 65% of initial activity
NADH
-
competitive
nitrate
sulfite
Zn2+
1 mM, about 35% of initial activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026 - 1
NAD+
0.004 - 2.51
NADP+
0.001 - 1.9
phosphite
0.0073 - 19.4
phosphonate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 5.7
NAD+
1.4 - 2.2
NADP+
0.0126 - 7.5
phosphite
0.041 - 8
phosphonate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00211 - 117
phosphonate
3397
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48 - 1.03
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
crude extract from Pseudomonas stutzeri
0.21
-
crude extract from Escherichia coli clone
3.49
pH 7.0, 25°C
5.2
-
purified enzyme from Pseudomonas stutzeri
6.52
-
purified enzyme from Escherichia coli clone
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
NaH2PO4/H3PO4 buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10
-
low activity
7
assay at, activity at pH 3.0 is about 2.2fold higher than at pH 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 50
-
25% of activity at 15°C, no activity at 50°C
20
about 13% of maximum activity
55
less than 10% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
isoelectric focusing, wild type enzyme
6.2
-
isoelectric focusing, A176R mutant enzyme; isoelectric focusing, E175A mutant enzyme
6.6
-
isoelectric focusing, E175A/A176R mutant enzyme
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
2 * 35000, SDS-PAGE
36400
-
x * 38500, SDS-PAGE, His-tag fusion protein, x * 36400, SDS-PAGE, native protein
69000
-
gel filtration
70000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of the electrostatic potentials of the interfaces between the subunits. Regions A, B, and C are almost electroneutral
mutant D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D, to 2.3 A resolution. The TS-PTDH monomer may be divided into a large and a small domain, separated by a flexible hinge region. The NAD+ cofactor is housed at the junction between the two domains, where residues from the large subunit engage in interactions with the ligand. In the cocrystal structure with NAD+ and inhibitor sulfite, the sulfite anion is situated proximal to the nicotinamide of the cofactor, where it is engaged through interactions with the side chains of Arg237, His292, and the backbone amides of Lys76 and Gly77
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10.5
1 h, more than 80% residual activity
726694
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39
-
wild-type, melting temperature
40
stable below
40.5
-
rapid inactivation, half life less than 10 min, 1 mM NAD+ partially protects against thermal inactivation, E175A/A176R double mutant is readily protected against inactivation by addition of 1 mM NADP+ for at least 15 min
55
complete inactivation
59.3
-
mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V, melting temperature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 20% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by small-scale protein purification
-
on Ni2+ affinity resin
-
recombinant and native protein
-
recombinant enzymes using His-tag
-
recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
His6-tagged PTDH overexpressed in Escherichia coli BL21(DE3) harboring a pET15b vector
-
in Escherichia coli
-
mutants cloned into pET15b as a N-terminal His-tagged construct
-
wild type and mutant proteins expressed in Escherichia coli BL21(DE3) as His-tag fusion protein
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
-
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
-
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
-
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
-
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
A146S
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 8 min
A176R
-
strongly decreased Km for NADP+
A319E
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
A319E/T101A
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 5 min
A325V
-
thermostability almost identical to that of the wild-type enzyme
C336D
-
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
D13E
-
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
D13E/M26I/E175A/E332N/C336D
-
mutant obtained by directed evolution, round 4
D13E/M26I/E175A/T181S/A308T/E332N/C336D
-
mutant obtained by directed evolution, round 6, strong decrease in KM value for NADP compared to wild-type
D13E/M26I/E175A/T181S/E332N/C336D
-
mutant obtained by directed evolution, round 5
D13E/M26I/E332N/C336D
-
mutant obtained by directed evolution, round 3
D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D
-
thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity. Mutation E175A leads to relaxation of cofactor specificity
D79A
-
significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates
D79N
-
has kinetic parameters more similar to those of wild-type
E130K
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 12.5 min
E130Q
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 7 min
E130R
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min
E175A/A176R
E332N
-
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
F198I
-
leads to low activity
F198M
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
H292Q
-
no activity, NAD+ binding is abolished
I313L
-
thermostability almost identical to that of the wild-type enzyme
K330*
-
mutant obtained by directed evolution, round 1
K76C
-
significant increase in Km for both substrates
K76M
-
significant increase in Km for both substrates
K76R
-
significant increase in Km for both substrates
L276C
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 12 min
L276H
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
L276Q
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 3.5 min
L276R
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 8 min
L276S
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 3 min
M26I
-
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
M26I/E332N/C336D
-
mutant obtained by directed evolution, round 2
Q132K
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 3 min
Q132R/Q137R/I150F/Q215L/R275Q
-
thermostable mutant, half-life at 45°C 161 min compared to 1.4 min of wild-type
Q137H
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min
Q137R/I150F/Q215L/R275Q
-
thermostable mutant, half-life at 45°C 200 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/A319E
-
thermostable mutant, half-life at 45°C 567 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/D162N/V315A
-
thermostable mutant, half-life at 45°C 614 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q
-
thermostable mutant, half-life at 45°C 437 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A
-
thermostable mutant, half-life at 45°C 1421 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/A325V
-
thermostable mutant, half-life at 45°C 2315 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/E130K
-
thermostable mutant, half-life at 45°C 1515 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/I313L
-
thermostable mutant, half-life at 45°C 1765 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R
-
thermostable mutant, half-life at 45°C 2350 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V
-
thermostable mutant, half-life at 45°C 8440 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V/A176R
-
highly stable and active mutant engineered for regeneration of NADPH and enzyme membrane reactors
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/V71I
-
thermostable mutant, half-life at 45°C 2000 min compared to 1.4 min of wild-type
Q215M
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 2.5 min
R237H
-
almost complete loss of activity
R237L
-
almost complete loss of activity
R237Q
-
almost complete loss of activity
R275L
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
T101A
-
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min
V315A
-
thermostability almost identical to that of the wild-type enzyme
V71Ia
-
thermostability almost identical to that of the wild-type enzyme
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
E266Q
-
significant increase in Km for both substrates, increase in turnover
-
H292N
-
almost complete loss of activity
-
K76A
-
significant increase in Km for both substrates
-
K76M
-
significant increase in Km for both substrates
-
K76R
-
significant increase in Km for both substrates
-
E175A/A176R
-
double mutant, 3.6-fold higher efficiency with NAD+, 1000-fold higher efficiency with NADP+, 3-fold favor for NADP+ over NAD+ as cofactor
-
H292F
-
no activity, NAD+ binding is abolished
-
H292K
-
no activity, NAD+ binding is abolished
-
H292N
-
no activity, NAD+ binding is abolished
-
R237K
-
strong increase in Km for both substrates, reduced Vmax
-
D79A
-
significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates
-
E266Q
-
higher activity, steady-state and pre-steady-state rates are comparable
-
K76A
-
pre-steady-state rates are approximately the same as the steady-state rates
-
R237K
-
low activity, absence of a significant burst in the pre-steady-state
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis
additional information